TRI32_HUMAN - dbPTM
TRI32_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI32_HUMAN
UniProt AC Q13049
Protein Name E3 ubiquitin-protein ligase TRIM32
Gene Name TRIM32
Organism Homo sapiens (Human).
Sequence Length 653
Subcellular Localization Cytoplasm. Localized in cytoplasmic bodies, often located around the nucleus.
Protein Description Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo..
Protein Sequence MAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQARYKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAAAASHL
------CHHHHHHCC		13.05-
7Phosphorylation-MAAAAASHLNLDAL
-CHHHHHHCCCHHHH		24.6329255136
50UbiquitinationICRQCLEKLLASSIN
HHHHHHHHHHHHHCC		35.53-
66UbiquitinationVRCPFCSKITRITSL
CCCCHHHHHHHHCCH		49.64-
71PhosphorylationCSKITRITSLTQLTD
HHHHHHHCCHHCCCC		17.8820860994
72PhosphorylationSKITRITSLTQLTDN
HHHHHHCCHHCCCCC		27.3527050516
74PhosphorylationITRITSLTQLTDNLT
HHHHCCHHCCCCCEE		22.6928348404
139UbiquitinationGHCTLPVKEAAEERR
CCCCCCHHHHHHHHH		39.43-
152UbiquitinationRRRDFGEKLTRLREL
HHHHHHHHHHHHHHH		56.38-
167UbiquitinationMGELQRRKAALEGVS
HHHHHHHHHHHHHHC		39.95-
175UbiquitinationAALEGVSKDLQARYK
HHHHHHCHHHHHHHH		61.1121890473
182MalonylationKDLQARYKAVLQEYG
HHHHHHHHHHHHHHC		26.8526320211
182UbiquitinationKDLQARYKAVLQEYG
HHHHHHHHHHHHHHC		26.85-
204UbiquitinationDELARSRKFFTGSLA
HHHHHHHCHHHCCHH		46.1821890473
215UbiquitinationGSLAEVEKSNSQVVE
CCHHHHHHHCCHHCH		61.1821890473
241PhosphorylationQAVSRCDYFLAKIKQ
HHHHHCCHHHHHHHH		12.2422461510
245UbiquitinationRCDYFLAKIKQADVA
HCCHHHHHHHHHCHH		53.21-
247UbiquitinationDYFLAKIKQADVALL
CHHHHHHHHHCHHHH		38.4321890473
257PhosphorylationDVALLEETADEEEPE
CHHHHHCCCCCCCCC		29.9928348404
268PhosphorylationEEPELTASLPRELTL
CCCCHHHCCCCEEEH		33.4024719451
274PhosphorylationASLPRELTLQDVELL
HCCCCEEEHHHEEEE		20.02-
282UbiquitinationLQDVELLKVGHVGPL
HHHEEEEEECCCCCC		59.8121890473
296UbiquitinationLQIGQAVKKPRTVNV
CCCCCCCCCCCEECC		61.14-
297UbiquitinationQIGQAVKKPRTVNVE
CCCCCCCCCCEECCC		32.88-
300PhosphorylationQAVKKPRTVNVEDSW
CCCCCCCEECCCCCH		25.5922210691
306PhosphorylationRTVNVEDSWAMEATA
CEECCCCCHHHHHHC		11.8320068231
312PhosphorylationDSWAMEATASAASTS
CCHHHHHHCHHHCCE		14.0820068231
314PhosphorylationWAMEATASAASTSVT
HHHHHHCHHHCCEEE		21.7320068231
317PhosphorylationEATASAASTSVTFRE
HHHCHHHCCEEEEEE		22.4120068231
318PhosphorylationATASAASTSVTFREM
HHCHHHCCEEEEEEC		23.6120068231
319PhosphorylationTASAASTSVTFREMD
HCHHHCCEEEEEECC		19.3720068231
321PhosphorylationSAASTSVTFREMDMS
HHHCCEEEEEECCCC		19.4220068231
328PhosphorylationTFREMDMSPEEVVAS
EEEECCCCHHHHCCC		25.5425159151
335PhosphorylationSPEEVVASPRASPAK
CHHHHCCCCCCCHHH		11.8729255136
339PhosphorylationVVASPRASPAKQRGP
HCCCCCCCHHHHCCH		27.0330278072
342UbiquitinationSPRASPAKQRGPEAA
CCCCCHHHHCCHHHH		43.86-
359UbiquitinationIQQCLFLKKMGAKGS
HHHHHHHHHCCCCCC		33.12-
360UbiquitinationQQCLFLKKMGAKGST
HHHHHHHHCCCCCCC		44.72-
393PhosphorylationLVADRGNYRIQVFTR
EEEECCCEEEEEEEC		16.3622210691
401UbiquitinationRIQVFTRKGFLKEIR
EEEEEECCCHHHHHH		51.46-
405UbiquitinationFTRKGFLKEIRRSPS
EECCCHHHHHHCCCC		49.1621890473
448PhosphorylationLIGVTDSYDNSLKVY
EEEECCCCCCCEEEE		23.1926437602
471UbiquitinationCHRSQLSKPWGITAL
ECHHHCCCCCCCEEC		54.0721890473
506UbiquitinationDRGSGVVKYSCLCSA
ECCCCEEEEEEEECC		29.10-
507PhosphorylationRGSGVVKYSCLCSAV
CCCCEEEEEEEECCC		7.9429496907
570PhosphorylationRQISHFFSENEDFRC
HHHHHHCCCCCCCCE		38.27-
604UbiquitinationKEILHFPKGGGYSVL
CEEECCCCCCCEEEE		70.06-
617PhosphorylationVLIREGLTCPVGIAL
EEEECCCCCCCEEEE		26.14-
627UbiquitinationVGIALTPKGQLLVLD
CEEEECCCCCEEEEE		54.79-
644PhosphorylationDHCIKIYSYHLRRYS
HHHHHHHHHHHHCCC		15.0023882029
645PhosphorylationHCIKIYSYHLRRYST
HHHHHHHHHHHCCCC		6.4729514088
650PhosphorylationYSYHLRRYSTP----
HHHHHHCCCCC----		15.5129514088
651PhosphorylationSYHLRRYSTP-----
HHHHHCCCCC-----		32.1829514088
652PhosphorylationYHLRRYSTP------
HHHHCCCCC------		24.8824719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
328SPhosphorylationKinaseCDK1P06493
PSP
335SPhosphorylationKinaseCDK1P06493
PSP
339SPhosphorylationKinaseCDK1P06493
PSP
651SPhosphorylationKinasePRKACAP36887
GPS
-KUbiquitinationE3 ubiquitin ligaseTRIM32Q13049
PMID:17987106
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI32_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TRI32_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQL1_HUMANUBQLN1physical
16189514
TRI32_HUMANTRIM32physical
11331580
TRIM1_HUMANMID2physical
11331580
TRI23_HUMANTRIM23physical
11331580
TRI27_HUMANTRIM27physical
11331580
ABI2_HUMANABI2physical
18632609
TRI32_HUMANTRIM32physical
17994549
UBE2N_HUMANUBE2Nphysical
17994549
PIAS4_HUMANPIAS4physical
16816390
TRI32_HUMANTRIM32physical
21628460
XIAP_HUMANXIAPphysical
21628460
RARA_HUMANRARAphysical
21984809
RXRA_HUMANRXRAphysical
21984809
UB2E2_HUMANUBE2E2physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UB2E3_HUMANUBE2E3physical
21143188
UBE2N_HUMANUBE2Nphysical
21143188
UB2V1_HUMANUBE2V1physical
21143188
UB2V2_HUMANUBE2V2physical
21143188
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
STING_HUMANTMEM173physical
22745133
DDX58_HUMANDDX58physical
22745133
DTBP1_HUMANDTNBP1physical
19349376
TRI32_HUMANTRIM32physical
19349376
UB2E1_HUMANUBE2E1physical
19349376
UB2D1_HUMANUBE2D1physical
22745133
UB2D3_HUMANUBE2D3physical
22745133
UBC_HUMANUBCphysical
23408431
UB2D1_HUMANUBE2D1physical
23408431
UB2D2_HUMANUBE2D2physical
23408431
UB2D3_HUMANUBE2D3physical
23408431
1433T_HUMANYWHAQphysical
23444366
1433F_HUMANYWHAHphysical
23444366
1433B_HUMANYWHABphysical
23444366
1433G_HUMANYWHAGphysical
23444366
1433E_HUMANYWHAEphysical
23444366
1433Z_HUMANYWHAZphysical
23444366
1433S_HUMANSFNphysical
23444366
TRI32_HUMANTRIM32physical
23444366
P73_HUMANTP73physical
23828567
TRI32_HUMANTRIM32physical
22493164
RN208_HUMANRNF208physical
22493164
VPS11_HUMANVPS11physical
22493164
TRI27_HUMANTRIM27physical
22493164
RNF41_HUMANRNF41physical
22493164
GLIS2_HUMANGLIS2physical
24500717
MYCN_HUMANMYCNphysical
25100564
P53_HUMANTP53physical
25146927
TRI32_HUMANTRIM32physical
16816390
UB2E1_HUMANUBE2E1physical
16816390
UB2D1_HUMANUBE2D1physical
16816390
TRI32_HUMANTRIM32physical
25416956
UBQL1_HUMANUBQLN1physical
25416956
KCTD9_HUMANKCTD9physical
25416956
CLIP4_HUMANCLIP4physical
25416956
PTCD2_HUMANPTCD2physical
25416956
SYT6_HUMANSYT6physical
25416956
UBE2U_HUMANUBE2Uphysical
25416956
UTER_HUMANSCGB1A1physical
21516116
NDRG2_HUMANNDRG2physical
25701873
TRI72_HUMANTRIM72physical
25701873
UB2D1_HUMANUBE2D1physical
25701873
UB2D2_HUMANUBE2D2physical
25701873
UB2D3_HUMANUBE2D3physical
25701873
S23IP_HUMANSEC23IPphysical
28514442
S23IP_HUMANSEC23IPphysical
27173435
TP4AP_HUMANTRPC4APphysical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
EXOC1_HUMANEXOC1physical
27173435
EXOC3_HUMANEXOC3physical
27173435
HSP74_HUMANHSPA4physical
28052117
1433F_HUMANYWHAHphysical
28052117
IQCB1_HUMANIQCB1physical
28498859
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
254110Limb-girdle muscular dystrophy 2H (LGMD2H)
615988Bardet-Biedl syndrome 11 (BBS11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI32_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-339, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-335 ANDSER-339, AND MASS SPECTROMETRY.

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